The association between high molecular weight glutenin subunit compositions and the bread-making quality of Chinese and Japanese hexaploid wheats

2000 ◽  
Vol 51 (3) ◽  
pp. 371 ◽  
Author(s):  
H. Nakamura
Keyword(s):  
Molecular Weight ◽  
Genetic Variation ◽  
High Molecular Weight ◽  
Hexaploid Wheat ◽  
Allelic Variation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Wheat Varieties ◽  
Hmw Glutenin

Variation in the electrophoretic banding patterns of high molecular weight (HMW) glutenin subunits of 274 hexaploid wheat (Triticum aestivum) varieties from China was examined by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Twenty-seven different major glutenin HMW subunits were identified. Each variety contained 3–5 subunits and 29 different glutenin subunit patterns were segregated. Seventeen alleles were identified based on comparison of subunit mobilities with those previously found for hexaploid wheat. Chinese hexaploid wheats exhibited particular allelic variation in glutenin HMW subunit composition and this variation differed from that found in wheats from Japanese and other countries. Average Glu-1 quality scores of 274 Chinese wheat varieties in the present study have been shown to be higher than that of Japanese wheats. Considerable genetic variation in the HMW glutenin subunit compositions of the Chinese wheats was observed in the present study and previously. Alleles from Chinese hexaploid wheat varieties have not been extensively introduced into Japan and other countries. The present data may indicate possible applications of Chinese germplasm in wheat breeding programs. To improve the wheat quality, genetic variation should be attempted through the introduction of genes of Chinese varieties into varieties in Japan and other countries.

The high-molecular-weight glutenin subunit composition of Japanese hexaploid wheat landraces

2000 ◽  
Vol 51 (6) ◽  
pp. 673 ◽  
Author(s):  
H. Nakamura
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Hexaploid Wheat ◽  
Storage Proteins ◽  
Allelic Variation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Subunit Composition ◽  
Wheat Landraces

The endosperm storage proteins of 174 Japanese wheat (Triticum aestivum) landraces were fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis to determine their high-molecular-weight (HMW) glutenin subunit composition. These are alleles for complex gene loci, Glu-A1, Glu-B1, and Glu-D1, that are present in Japanese hexaploid wheat landraces. These were identified by comparison with the subunit mobility previously found in hexaploid wheat. Twenty-four different, major glutenin HMW subunits were identified. Each landrace contained 3–5 subunits, and 17 different glutenin subunit patterns were observed for 13 alleles in Japanese landraces. Japanese landraces showed specific allelic variation in glutenin HMW subunits, different from those in non-Japanese hexaploid wheats.

The high-molecular-weight glutenin subunit composition of Australian wheat cultivars

1986 ◽  
Vol 37 (2) ◽  
pp. 125 ◽  
Author(s):  
GJ Lawrence
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Storage Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Subunit Composition ◽  
Wheat Cultivars ◽  
Australian Wheat ◽  
Hmw Glutenin

The seed storage proteins of 106 Australian wheat cultivars were fractionated by sodium dodecyl sulfate polyacrylamide gel electrophoresis to determine the allelic composition of the cultivars at each of the three loci controlling high-molecular-weight (HMW) glutenin subunits. Amongst the cultivars, three alleles were identified at the Glu-A1 locus, eight at the Glu-B1locus and four at the Glu-D1 locus. The results are presented in the form of a key to aid identification of unknown samples. Sixteen of the cultivars were found to consist of two or more biotypes with respect to HMW glutenin subunit composition.

scholarly journals The high-molecular-weight glutenin subunit compositions of wheat varieties bred in Finland

1986 ◽  
Vol 58 (4) ◽  
pp. 151-156
Author(s):  
Tuula Sontag ◽  
Hannu Salovaara ◽  
Peter I Payne
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Bread Wheat ◽  
Polyacrylamide Gel Electrophoresis ◽  
Glutenin Subunit ◽  
Bread Making ◽  
Wheat Varieties ◽  
Hmw Glutenin Subunit ◽  
Hmw Glutenin

The composition of high-molecular-weight (HMW) glutenin subunits in 35 Finnish bread wheat cultivars was determined by SDS-polyacrylamide gel electrophoresis. One third of the varieties have one of two HMW glutenin subunit compositions and there are only 17 different compositions in all. Three cultivars, Antti, Kiuru and Panu, are genetically mixed for some of these subunits. Cultivar Tammi (II) contains a novel HMW subunit of glutenin, not detected in any bread wheat previously analysed, and is presumed to be coded by genes on chromosome 1A at the Glu-A1 locus. On the basis of previous work, which related individual subunits to bread-making quality, HMW glutenin subunit quality (Glu-1 quality) scores were calculated for the varieties. The results are related to the bread-making quality of Finnish wheats.

Characterization of 1Sty13, a novel high-molecular-weight glutenin subunit from Elymus sibiricus L.

2021 ◽  
pp. 1-4
Author(s):  
Mei Yan ◽  
Muzi Li ◽  
Zaidong Yang ◽  
Feng Yu ◽  
Xuye Du
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Glutenin Subunit ◽  
Predicted Amino Acid Sequence ◽  
Reading Frame ◽  
Elymus Sibiricus ◽  
Dough Quality ◽  
Key Factor

Abstract High-molecular-weight glutenin subunit (HMW-GS) is a key factor affecting dough-processing quality. 1Sty13 is a novel HMW-GS found in the tetraploid species, Elymus sibiricus L. 1Sty13 has faster electrophoretic mobility than the 1Dy12 subunit on sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis. The gene encoding the 1Sty13 subunit was composed of 1803 nucleotide base pairs with an open reading frame that was 599 amino acids in length. Analysis of the predicted amino acid sequence of 1Sty13 indicated that the N-terminal domain was similar to the y-type subunit, whereas the C-terminal domains were similar to the x-type subunit. Five cysteine residues were found in 1Sty13, which is one less than the published HMW-GS in the St genome. The 1Sty13 protein was purified at a scale sufficient for incorporation into flour for the SDS sedimentation test, which indicated that incorporating 1Sty13 improved dough quality.

scholarly journals The interrelations between high- and low-molecular-weight forms of normal and mutant (Krabbe-disease) galactocerebrosidase

1980 ◽  
Vol 189 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Yoav Ben-Yoseph ◽  
Melinda Hungerford ◽  
Henry L. Nadler
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Active Form ◽  
Sodium Dodecyl ◽  
Krabbe Disease ◽  
Low Molecular Weight ◽  
Molecular Weight Form

Galactocerebrosidase (β-d-galactosyl-N-acylsphingosine galactohydrolase; EC 3.2.1.46) activity of brain and liver preparations from normal individuals and patients with Krabbe disease (globoid-cell leukodystrophy) have been separated by gel filtration into four different molecular-weight forms. The apparent mol.wts. were 760000±34000 and 121000±10000 for the high- and low-molecular-weight forms (peaks I and IV respectively) and 499000±22000 (mean±s.d.) and 256000±12000 for the intermediate forms (peaks II and III respectively). On examination by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, the high- and low-molecular-weight forms revealed a single protein band with a similar mobility corresponding to a mol.wt. of about 125000. Antigenic identity was demonstrated between the various molecular-weight forms of the normal and the mutant galactocerebrosidases by using antisera against either the high- or the low-molecular-weight enzymes. The high-molecular-weight form of galactocerebrosidase was found to possess higher specific activity toward natural substrates when compared with the low-molecular-weight form. It is suggested that the high-molecular-weight enzyme is the active form in vivo and an aggregation process that proceeds from a monomer (mol.wt. approx. 125000) to a dimer (mol.wt. approx. 250000) and from the dimer to either a tetramer (mol.wt. approx. 500000) or a hexamer (mol.wt. approx. 750000) takes place in normal as well as in Krabbe-disease tissues.

scholarly journals Evaluation of winter wheat collection in terms of HMW- and LMW-glutenin subunits

2010 ◽  
Vol 46 (Special Issue) ◽  
pp. S96-S99 ◽  
Author(s):  
J. Bradová ◽  
L. Štočková
Keyword(s):  
Molecular Weight ◽  
Winter Wheat ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Low Molecular Weight ◽  
Glutenin Subunits ◽  
Bread Making ◽  
Wheat Varieties ◽  
Lmw Glutenin Subunits ◽  
Winter Wheat Varieties

The composition of high molecular weight (HMW-GS) and low molecular weight (LMW-GS) glutenin subunits was examined in a collection of 86 Czech registered winter wheat varieties. These proteins were analyzed by sodium dodecyl sulphate polyacrylamide gel electrophoresis. An inter-varietal polymorphism of the HMW and LMW glutenin subunits was detected. Twenty-one different patterns for HMW were identified, and eighteen for the LMW-glutenins. The different alleles encoded at the six glutenin loci were determined. Three, six, and four alleles were observed, respectively at the <I>Glu-A1, Glu-</I>B1, and <I>Glu-D1 </I>loci (encoding high HMW-GS). Three, eight, and three alleles of LMW-GS were found, respectively, at the <I>Glu-A3, Glu- B3</I>, and <I>Glu-D3 </I>loci. The evaluated varieties were split into four categories of baking quality, and these variety groups were analyzed for the presence of different HMW-GS and LMW-GS alleles. While the alleles <I>Glu-B1c </I>(7+9), and <I>Glu-D1d </I>(5+10) were detected exclusively in bread wheat varieties, the alleles <I>Glu-B1d </I>(6+8), <I>Glu-D1a </I>(2+12), and <I>Glu-A3e/f </I>only occurred in those varieties that are not suitable for bread-making. &nbsp;

Genetic variation of high-molecular-weight glutenin subunit composition in Asian wheat

2010 ◽  
Vol 58 (2) ◽  
pp. 283-289 ◽  
Author(s):  
Yohei Terasawa ◽  
Kanenori Takata ◽  
Hisashi Hirano ◽  
Kenji Kato ◽  
Taihachi Kawahara ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Genetic Variation ◽  
High Molecular Weight ◽  
Glutenin Subunit ◽  
Subunit Composition

scholarly journals High-molecular weight kininogen is present in cultured human endothelial cells: localization, isolation, and characterization

Blood ◽  
1988 ◽  
Vol 71 (5) ◽  
pp. 1268-1276 ◽  
Author(s):  
F van Iwaarden ◽  
PG de Groot ◽  
JJ Sixma ◽  
M Berrettini ◽  
BN Bouma
Keyword(s):  
Molecular Weight ◽  
Endothelial Cells ◽  
Endothelial Cell ◽  
High Molecular Weight ◽  
Light Chain ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Enzyme Linked Immunosorbent Assay ◽  
Human Endothelial Cells ◽  
Isolation And Characterization

Abstract The presence of high-molecular weight (mol wt) kininogen was demonstrated in cultured human endothelial cells derived from the umbilical cord by immunofluorescence techniques. Cultured human endothelial cells contain 58 +/- 11 ng (n = 16) high-mol wt kininogen/10(6) cells as determined by an enzyme-linked immunosorbent assay (ELISA) specific for high-mol wt kininogen. High-mol wt kininogen was isolated from cultured human endothelial cells by immunoaffinity chromatography. Nonreduced sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that endothelial cell high-mol wt kininogen consisted of five protein bands with mol wts of 95,000, 85,000, 65,000, 46,000, and 30,000 daltons. Immunoblotting of the endothelial cell high-mol wt kininogen by using specific antisera against the heavy and light chain indicated that the 95,000-, 85,000-, and 65,000-dalton bands consisted of the heavy and light chain whereas the 46,000- and 30,000-dalton bands reacted only with the anti-light chain antiserum. Immunoprecipitation studies performed with lysed, metabolically labeled endothelial cells and monospecific antisera directed against high-mol wt kininogen suggested that high-mol wt kininogen is not synthesized by the endothelial cells. Endothelial cells cultured in high-mol wt kininogen-free medium did not contain high-mol wt kininogen. These studies indicate that endothelial cell high-mol wt kininogen was proteolytically cleaved in the culture medium and subsequently internalized by the endothelial cells. Binding and internalization studies performed with 125I-labeled, proteolytically cleaved, high-mol wt kininogen showed that endothelial cells can indeed bind and internalize proteolytically cleaved high-mol wt kininogen in a specific and saturable way.

Genetic diversity of high-molecular-weight glutenin subunit compositions in bread wheat landraces originated from Turkey

2016 ◽  
Vol 16 (1) ◽  
pp. 28-38 ◽  
Author(s):  
Ridvan Temizgul ◽  
Mikail Akbulut ◽  
Domenico Lafiandra
Keyword(s):  
Genetic Diversity ◽  
Molecular Weight ◽  
Genetic Variation ◽  
High Molecular Weight ◽  
Bread Wheat ◽  
Gene Diversity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Genetic Erosion ◽  
Allele Polymorphism ◽  
Wheat Landraces

AbstractFocusing on 116 bread wheat landraces, this study investigated high molecular weight glutenin allele polymorphism, gene diversity, genetic variation and linkage disequilibrium (LD) inGlu-1loci. To identify gluten alleles, sodium dodesyl sulphate-polyacrylamide, gel electrophoresis was used and for statistical analyses POPGENE software was employed. The results indicated that average genetic variation (h) was the highest inGlu-B1(0.6421) and the lowest inGlu-A1locus (0.4548); genetic similarity ratio (I) was the highest inGlu-B1(1.4170); the highest average genetic diversity (Ht) was observed inGlu-B1(0.6575) and the lowest diversity was observed inGlu-A1(0.4558). It was also observed that genetic diversity inGlu-1locus was largely due to intra-population variations. Inter-population gene flow was also calculated as 4.0051. Marmara and Southeastern Anatolia regions, the results further indicated, had the highest (2.8691) and lowest (0.1694) heterozygosity. Genetic erosion risk for Turkish bread wheat landraces was also seen to be high. Considering the mutual analyses of subunits of nationwide wheat landraces, it is possible to speculate about a limited migration between the landraces. LD of the landraces was largely because of this limited migration and/or epistatic natural selection. Since Turkey is known as the gene centre for major cereals including wheat, barley, rye and oat, where they diversified and spread throughout the world, studying the gluten allele diversity of Turkish bread wheat landraces is important. In addition, this study has revealed the applicability of LD, and neutrality tests to gluten protein diversity for the first time.

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